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Conserved domains on  [gi|502647475|ref|WP_012883795|]
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Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK [Dickeya parazeae]

Protein Classification

aminoacyl-tRNA deacylase( domain architecture ID 10793438)

aminoacyl-tRNA deacylase of the YbaK/EbsC family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 3.30e-96

Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;


:

Pssm-ID: 182634  Cd Length: 159  Bit Score: 274.70  E-value: 3.30e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   1 MTPAVKLLEKQKITFTLHSYHHDADETNFGEEAARKLGLDKQQVYKTLLVSLNGDAKQLAVAVTPVASQLDLKKVAKALA 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502647475  81 AKKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIAKHD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
 
Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 3.30e-96

Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;


Pssm-ID: 182634  Cd Length: 159  Bit Score: 274.70  E-value: 3.30e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   1 MTPAVKLLEKQKITFTLHSYHHDADETNFGEEAARKLGLDKQQVYKTLLVSLNGDAKQLAVAVTPVASQLDLKKVAKALA 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502647475  81 AKKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIAKHD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 1.07e-68

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 204.61  E-value: 1.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   1 MTPAVKLLEKQKITFTLHSYHHDaDETNFGEEAARKLGLDKQQVYKTLLVslNGDAKQLAVAVTPVASQLDLKKVAKALA 80
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHD-EDASDGLEAAEKLGLDPEQVFKTLVV--EGDKKGLVVAVVPVDEELDLKKLAKALG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502647475  81 AKKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADI 155
Cdd:cd00002   78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 3.45e-56

Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272853 [Multi-domain]  Cd Length: 152  Bit Score: 173.19  E-value: 3.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475    2 TPAVKLLEKQKITFTLHSYHHDADETnFGEEAARKLGLDKQQVYKTLLvsLNGDAKQLAVAVTPVASQLDLKKVAKALAA 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLV--AEGDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502647475   82 KKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIA 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-159 5.54e-48

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 152.17  E-value: 5.54e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   2 TPAVKLLEKQKITFTLHSYhhdADETNFGEEAARKLGLDKQQVYKTLLVSLNGdakQLAVAVTPVASQLDLKKVAKALAA 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDG---GPVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502647475  82 KKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIAKHD 159
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 31-146 1.98e-13

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 63.00  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   31 EEAARKLGLDKQQVYKTLLVSlnGDAKQLAVAVTPVASQLDLKKVAKALAAKKADMADPQLAQRVTGYLVGGISPLG-QK 109
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLK--DKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKA 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 502647475  110 KLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLAN 146
Cdd:pfam04073  86 KGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRK 122
 
Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 3.30e-96

Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;


Pssm-ID: 182634  Cd Length: 159  Bit Score: 274.70  E-value: 3.30e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   1 MTPAVKLLEKQKITFTLHSYHHDADETNFGEEAARKLGLDKQQVYKTLLVSLNGDAKQLAVAVTPVASQLDLKKVAKALA 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502647475  81 AKKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIAKHD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 1.07e-68

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 204.61  E-value: 1.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   1 MTPAVKLLEKQKITFTLHSYHHDaDETNFGEEAARKLGLDKQQVYKTLLVslNGDAKQLAVAVTPVASQLDLKKVAKALA 80
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHD-EDASDGLEAAEKLGLDPEQVFKTLVV--EGDKKGLVVAVVPVDEELDLKKLAKALG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502647475  81 AKKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADI 155
Cdd:cd00002   78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 3.45e-56

Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272853 [Multi-domain]  Cd Length: 152  Bit Score: 173.19  E-value: 3.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475    2 TPAVKLLEKQKITFTLHSYHHDADETnFGEEAARKLGLDKQQVYKTLLvsLNGDAKQLAVAVTPVASQLDLKKVAKALAA 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLV--AEGDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502647475   82 KKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIA 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-159 5.54e-48

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 152.17  E-value: 5.54e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   2 TPAVKLLEKQKITFTLHSYhhdADETNFGEEAARKLGLDKQQVYKTLLVSLNGdakQLAVAVTPVASQLDLKKVAKALAA 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDG---GPVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502647475  82 KKADMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIAKHD 159
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 18-153 2.83e-30

YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).


Pssm-ID: 239824 [Multi-domain]  Cd Length: 136  Bit Score: 106.47  E-value: 2.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475  18 HSYHHDADeTNFGEEAARKLGLDKQQVYKTLLVSlnGDAKQLAVAVTPVASQLDLKKVAKALAAKKADMADPQLAQRVTG 97
Cdd:cd04332    3 LEYEHTPG-AKTIEEAAEALGVPPGQIAKTLVLK--DDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502647475  98 YLVGGISPLGQKKLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLK-AQFA 153
Cdd:cd04332   80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGeAEVA 136
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 31-146 1.98e-13

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 63.00  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   31 EEAARKLGLDKQQVYKTLLVSlnGDAKQLAVAVTPVASQLDLKKVAKALAAKKADMADPQLAQRVTGYLVGGISPLG-QK 109
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLK--DKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKA 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 502647475  110 KLLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLAN 146
Cdd:pfam04073  86 KGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRK 122
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 5-156 3.63e-10

YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 55.04  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475   5 VKLLEKQKITFTLhsYHHDADETNfgEEAARKLGLDKQQVYKTLLVSLNGDAKQLAVAVTPVASQLDLKKVAKALAAKKA 84
Cdd:cd04336    5 QELLNTNGARFRV--LDHPPEGTS--EEVAAIRGTELGQGAKALLCKVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502647475  85 DMADPQLAQRVTGYLVGGISPLGQKKLLPTVIDEG-AQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADIA 156
Cdd:cd04336   81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSlLDRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQFT 153
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 31-155 6.02e-09

This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.


Pssm-ID: 239825 [Multi-domain]  Cd Length: 148  Bit Score: 51.73  E-value: 6.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502647475  31 EEAARKLGLDKQQVYKTLLVSLNGDAkqlAVAVTPVASQLDLKKVAKALAAKKaDMADPQLAQRVTGYLVGGISPLGQKK 110
Cdd:cd04333   28 ALAAEALGCEPGQIAKSLVFRVDDEP---VLVVTSGDARVDNKKFKALFGEKL-KMADAEEVRELTGFAIGGVCPFGHPE 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502647475 111 LLPTVIDEGAQQFGTIFVSGGKRGLDLELAATDLANVLKAQFADI 155
Cdd:cd04333  104 PLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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